Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme

Tadashi Ueda, Takatoshi Ohkuri, Taiji Imoto

Research output: Contribution to journalArticle

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Abstract

We prepared three peptide fragments (fg.59-105, fg.63-105 and fg.64-105) by the BrCN cleavage of mutant lysozymes where Ile58, Trp62 and Trp63 were mutated to Met, respectively. From the analysis of formation of the disulfide bonds among Cys64, Cys76, Cys80 and Cys94 in the renaturation of each peptide fragment from the reduced form, Trp62 and Trp63 were required for the effective formation of two disulfide bonds. Especially, Trp62 was found to be involved in the correct formation of the disulfide bonds.

Original languageEnglish
Pages (from-to)203-208
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume228
Issue number1
DOIs
Publication statusPublished - Nov 1 1996

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Muramidase
Disulfides
Conformations
Peptide Fragments
Peptides

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme. / Ueda, Tadashi; Ohkuri, Takatoshi; Imoto, Taiji.

In: Biochemical and Biophysical Research Communications, Vol. 228, No. 1, 01.11.1996, p. 203-208.

Research output: Contribution to journalArticle

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